These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Lysophospholipase activity of bovine adrenal medulla. A reevaluation.
    Author: Franson RC, Van den Bosch H.
    Journal: Biochim Biophys Acta; 1982 Apr 15; 711(1):75-82. PubMed ID: 7066375.
    Abstract:
    1. Chromaffin granule preparations isolated from bovine adrenal medulla hydrolyzed endogenous lysophosphatidylcholine (lyso-PC) and generated lysophosphatidylethanolamine when dialyzed at pH 7.5. 2. Undialyzed granule preparations hydrolyzed exogenously added [1-14C]palmitoyl-lyso-PC maximally (12-16 nmol/min per mg) at pH 7.5. At a given concentration of protein, activity increased with increasing concentrations of substrate lyso-PC to a maximum beyond which substrate inhibited activity up to 95%. 3. More than 95% of the lysophospholipase activity of fresh granule preparations toward exogenously added lyso-PC was inactivated irreversibly by dialysis. 4. By contrast, fresh microsomal preparations from adrenal medulla had similar substrate requirements for maximal lysophospholipase activity, but more than 35% of the activity was retained at high substrate concentrations or after extensive dialysis. 5. We conclude that adrenal organelles, other than microsomes, contain potent membrane-associated lysophospholipase activity that is inactivated preferentially by high detergent-substrate concentrations and/or dialysis. These observations suggest that lysophospholipase activity (and perhaps phospholipase A activity) is more widely distributed in organelle membranes of the adrenal medulla than was reported previously.
    [Abstract] [Full Text] [Related] [New Search]